Structure of PDB 1cvl Chain A

Receptor sequence
>1cvlA (length=316) Species: 42739 (Chromobacterium viscosum) [Search protein sequence]
ADTYAATRYPVILVHGLAGTDKFANVVDYWYGIQSDLQSHGAKVYVANLS
GFQSDDGPNGRGEQLLAYVKQVLAATGATKVNLIGHSQGGLTSRYVAAVA
PQLVASVTTIGTPHRGSEFADFVQDVLKTDPTGLSSTVIAAFVNVFGTLV
SSSHNTDQDALAALRTLTTAQTATYNRNFPSAGLGAPGSCQTGAATETVG
GSQHLLYSWGGTAIQPTSTVTGATDTSTGTLDVANVTDPSTLALLATGAV
MINRASGQNDGLVSRCSSLFGQVISTSYHWNHLDEINQLLGVRGANAEDP
VAVIRTHVNRLKLQGV
3D structure
PDB1cvl Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6 angstroms resolution.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L17 S87 Q88 D241 D263 H285 D287 Q291 V295
Catalytic site (residue number reindexed from 1) L17 S87 Q88 D238 D260 H282 D284 Q288 V292
Enzyme Commision number 3.1.1.3: triacylglycerol lipase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 CA A D241 D287 Q291 V295 D238 D284 Q288 V292
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004806 triacylglycerol lipase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0016042 lipid catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function

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Cellular Component
External links
PDB RCSB:1cvl, PDBe:1cvl, PDBj:1cvl
PDBsum1cvl
PubMed8683577
UniProtP0DUB9|LIP_PSEPS Triacylglycerol lipase (Gene Name=lip)

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